ID K9RSE9_SYNP3 Unreviewed; 341 AA.
AC K9RSE9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=ABC-type dipeptide/oligopeptide/nickel transport system, permease component {ECO:0000313|EMBL:AFY60466.1};
GN OrderedLocusNames=Syn6312_1285 {ECO:0000313|EMBL:AFY60466.1};
OS Synechococcus sp. (strain ATCC 27167 / PCC 6312).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=195253 {ECO:0000313|EMBL:AFY60466.1, ECO:0000313|Proteomes:UP000010379};
RN [1] {ECO:0000313|Proteomes:UP000010379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27167 / PCC 6312 {ECO:0000313|Proteomes:UP000010379};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU363032};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU363032}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000256|RuleBase:RU363032}.
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DR EMBL; CP003558; AFY60466.1; -; Genomic_DNA.
DR RefSeq; WP_015124010.1; NC_019680.1.
DR AlphaFoldDB; K9RSE9; -.
DR STRING; 195253.Syn6312_1285; -.
DR KEGG; syne:Syn6312_1285; -.
DR PATRIC; fig|195253.3.peg.1305; -.
DR eggNOG; COG0601; Bacteria.
DR HOGENOM; CLU_036879_0_0_3; -.
DR OrthoDB; 9773683at2; -.
DR Proteomes; UP000010379; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; MetI-like; 1.
DR InterPro; IPR045621; BPD_transp_1_N.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR PANTHER; PTHR43163; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR PANTHER; PTHR43163:SF6; DIPEPTIDE TRANSPORT SYSTEM PERMEASE PROTEIN DPPB-RELATED; 1.
DR Pfam; PF00528; BPD_transp_1; 1.
DR Pfam; PF19300; BPD_transp_1_N; 1.
DR SUPFAM; SSF161098; MetI-like; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363032};
KW Reference proteome {ECO:0000313|Proteomes:UP000010379};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363032};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363032};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU363032}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 108..129
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 141..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT TRANSMEM 313..335
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363032"
FT DOMAIN 102..332
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50928"
SQ SEQUENCE 341 AA; 37384 MW; 452697C4DC81F7CB CRC64;
MSRLRALQAY ILVRLLLAPL MLLTIVTIVF LLLRATPGDP VDAILGPRAP AAVKEALREQ
LGLAAPLWEQ YFKYLGQLLH LNLGTSLTSQ GEPVANIIQA HFPATAELAL YSLGLAFLIG
IGVGTVAAVK RNSVWDVGGR LFGIVTYALP LFWLGMLLQL VFAVELRWLP LGTRYPVTLP
PPQGWTGLYT IDSLLSGQWQ ELGISIYYLI LPTLSLAIVL SGIFERIVRV NLQQTLQSDY
VEAARARGIP EIKILFNHAL KNALIPVITV LGLTFASLLG GAVLTEVTFS WPGLGNRLYE
AISLRDYATV QGIMVFFAVV VVVVSLAIDI CNAWIDPRIR Y
//
